Recombinant Mouse pIgR Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Mouse pIgR Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse plgR is coated at 2 μg/mL (100 μL/well), the concentration of mouse IgM that produces 50% of the optimal binding response is 20-100 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse pIgR protein
Lys19-Lys645, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Lys19
Protein/Peptide Type
Recombinant Proteins
Gene
PIGR
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
70.1 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
93-97 kDa, reducing conditions
Publications
Read Publications using
2800-PG in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse pIgR Protein, CF

  • FLJ22667
  • hepatocellular carcinoma associated protein TB6
  • Hepatocellular carcinoma-associated protein TB6
  • MGC125361
  • MGC125362
  • pIgR
  • Poly-Ig receptor
  • polymeric immunoglobulin receptor

Background

The mouse polymeric immunoglobulin receptor (plgR; also known as membrane secretory component) is a 115 kDa type I transmembrane glycoprotein that is synthesized as a 771 amino acid (aa) precursor. It includes an 18 aa signal sequence, a 627 aa extracellular domain (ECD) (aa 19‑645), a 23 aa transmembrane segment (aa 646‑668), and a 143 aa cytoplasmic region (aa 669‑771) (1‑3). The ECD consists of five V-type Ig-like domains and a sixth non-Ig domain that connects to the transmembrane region. The ECD of mouse plgR is 65%, 69%, 85%, 62% and 62% aa identical to the equivalent region in human, porcine, rat, bovine and canine, respectively. plgR is expressed on secretory epithelial cells and serves as a carrier that transports IgA and IgM across epithelium (1, 2, 4). On the basolateral surface of epithelial cells, the receptor initially binds non-covalently to IgA via domains #1 and #5 of the plgR. A rearrangement then occurs where a disulfide bond forms between domain #5 of the plgR and an IgA heavy chain (2). This complex is then internalized and transcytosed to the apical surface. A soluble covalent complex called secretory IgA (SIgA) is generated by proteolytic cleavage of the complex in the sixth extracellular domain of plgR and released into the lumen (5). This proteolytically generated plgR fragment is referred to as secretory component (SC). Notably, in human, plgR transcytoses constitutively, with or without ligand, creating both a bound and free, 78 kDa SC following cleavage (3). In mouse, this event would be expected to generate a 95 kDa fragment (1). The receptor component of the complex anchors the SIgA molecule to mucous (6), where it serves to protect mucous membranes that form a barrier between the interior of the body and the external environment (7).

  1. de Groot, N. et al. (1999) Transgenic Res. 8:125.
  2. Piskurich, J. et al. (1995) J. Immunol. 154:1735.
  3. Brandtzaeg, P. and F-E. Johansen (2001) Trends Immunol. 22:545.
  4. Ben-Hur, H. et al. (2004) Int. J. Mol. Med. 14:35.
  5. Asano, M. et al. (2004) Immunology 112:583.
  6. Phalipon, A. and B. Corthesy (2003) Trends Immunol. 24:55.
  7. Uren, T. et al. (2003) J. Immunol. 170:2531.

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Bioinformatics

Gene Symbol PIGR
Uniprot